Human immunodeficiency virus type 1 and 2 envelope glycoproteins oligomerize through conserved sequences

J Virol. 1997 Jul;71(7):5706-11. doi: 10.1128/JVI.71.7.5706-5711.1997.

Abstract

Hetero-oligomerization between human immunodeficiency virus type 2 (HIV-2) envelope glycoprotein (Env) truncation mutants and epitope-tagged gp160 is dependent on the presence of gp41 transmembrane protein (TM) amino acids 552 to 589, a putative amphipathic alpha-helical sequence. HIV-2 Env truncation mutants containing this sequence were also able to form cross-type hetero-oligomers with HIV-1 Env. HIV-2/HIV-1 hetero-oligomerization was, however, more sensitive to disruption by mutagenesis or increased temperature. The conservation of the Env oligomerization function of the HIV-1 and HIV-2 alpha-helical sequences suggests that retroviral TM alpha-helical motifs may have a universal role in oligomerization.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • CD4 Antigens / metabolism
  • Conserved Sequence*
  • Gene Products, env / genetics
  • Gene Products, env / metabolism*
  • HIV Envelope Protein gp160 / genetics
  • HIV Envelope Protein gp160 / metabolism
  • HIV Envelope Protein gp41 / genetics
  • HIV Envelope Protein gp41 / metabolism*
  • HIV-1 / genetics
  • HIV-1 / metabolism*
  • HIV-2 / genetics
  • HIV-2 / metabolism*
  • HeLa Cells
  • Humans
  • Molecular Sequence Data
  • Sequence Deletion
  • Structure-Activity Relationship

Substances

  • CD4 Antigens
  • Gene Products, env
  • HIV Envelope Protein gp160
  • HIV Envelope Protein gp41